Proton transfer is the essence of acid-base catalysis and hence fundamental to the action of most enzymes. Bio-organic chemists have, therefore, directed an enormous amount of effort toward the attainment of a complete description of proton transfer reactions in water. Surprisingly, however, this work has largely neglected the powerful dynamic nmr method as a tool for studying proton transfers. Considering that proton transfer is an important and ofter rate-determining aspect of enzyme "model" systems, the scarcity of pmr data in bio-organic chemistry constitutes a sizeable void. In view of this situation, we propose to apply dynamic nmr to biologically interesting proton transfers as well as to other fast reactions. The work will include studies of amide proton exchange in both aqueous and non-aqueous solvents; of proton transfers at micelle surfaces; of the mechanism of proton exchange of hydrogen bonded alcohols; of molecular rotation of charge-transfer complexes. We will also undertake an investigation of proton transfer reactions of endo and exo-2-dimethylaminonorbornane, the results of which will have bearing on the orbital steering theory for enzyme action. BIBLIOGRAPHIC REFERENCES: F.M. Menger, G. Saito, G.V. Sanzero, and J.R. Dodd, J. Amer. Chem. Soc., 97, 909 (1975). "Motional Freedom and Polarity within Water Pools of Different Sizes. S in Label Studies". F.M. Menger, S. Wrenn, and H.K. Rhee, Bioorganic Chemistry, 4, 194 (1975). "Aminolysis of Oxalate Esters in Toluene. A model for a Carboxylate Buried in a Hydrocarbon Environment at an Active Site".